Peptic hydrolysis of Trypsin inhibited by DFP yielded a fragment distinguished by its Rf from a corresponding fragment of native enzyme and containing both tryptophane and phosphorus. DFP protects one Try of Trypsin and Chymotrypsin against Oxidation by N-Bromosuccinimid. Differencespectroscopy revealed corresponding changes in absorption spectra of Trypsin and Chymotrypsin the significance of which is discussed in detail. Electrophoretic mobility of the isolated fragment excludes dissociable phosphate groups, proving the presence of DIP-residue. Hydrolysis of the fragment yielded equimolar Try., Leu., Val., and Ser.
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